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Ultracentrifugation studies on the transmembrane domain of the human erythrocyte anion transporter Band 3 in the detergent C12E8 |
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| Authors: | H. Cölfen J. M. Boulter Stephen E. Harding Anthony Watts |
| Affiliation: | (1) Max-Planck-Institute of Colloids & Interfaces, Colloid Chemistry, Kantstrasse 55, D-14513 Teltow, Germany, e-mail: COELFEN@MPIKG-TELTOW.MPG.DE, DE;(2) Skirball Institute of Biomolecular Medicine, Structural Biology Program, New York University Medical Center, 540 First Avenue, NY 10016, USA, US;(3) NCMH Unit, University of Nottingham, School of Biological Sciences, Sutton Bonington, LE12 5RD, UK, GB;(4) Biomembrane Structure Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK, GB |
| Abstract: | The dilute solution behaviour of the transmembrane domain (TMD) of the human erythrocyte anion exchanger Band 3 was studied by analytical ultracentrifugation. Sedimentation velocity and equilibrium studies of the TMD solubilized with the detergent C12E8 demonstrate that the protein is a stable dimer in the concentration range 0.1 to 1 mg/ml. There is no evidence of a dissociation at low concentrations or of an association at higher concentrations. Hydrodynamic calculations applying a prolate ellipsoid of revolution and assuming a hydration of w=0.35 result in an asymmetrical particle with an axial ratio (a/b) of ∼3.5. Received: 8 January 1998 / Revised version: 21 April 1998 / Accepted: 22 April 1998 |
| Keywords: | Band 3 Membrane protein Analytical ultracentrifugation Hydrodynamics |
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